Many groups worldwide have a vested interest in inserting genes into Brassica napus in an effort to produce the industrial feedstock trierucin. Erucic acid (cis-13 docosenoic acid, 22:1) is the major very long chain fatty acid (VLCFA) in the seed oil from HEAR (high erucic acid rapeseed) Brassica napus cultivars, accounting for 45-55% of the total fatty acids (Han 2001). HEAR cultivars are of high interest for industrial purposes because 22:1 is a valuable feedstock with more than 1000 potential or patented industrial applications (Sontaag 1995; Scarth 2006). Currently the major derivative of erucic acid is erucamide, which is used as a surface-active additive in coatings and in the production of plastic films as an anti-block or slip agent. Many other applications are foreseen for erucic acid and its hydrogenated derivative behenic acid, e.g. in lubricants, detergents, film processing agents and coatings, as well as in cosmetics and pharamceuticals (Leonard 1993; Derksen 1995; McVetty 2002; Puyaubert 2005). For many of these industrial uses, the economics are limited by the proportion of 22:1 in the seed oil. To compete with petroleum-based products, it is desirable to increase the 22:1 proportion as high as possible in order to reduce the cost of purification (Scarth 2006). In addition, the engineering of HEAR Brassicaceae to produce seed oils containing substantial trierucin would lend the intact oil to a wide range of new applications (Sonntag 1995). In general, stereospecific analyses have shown that among most members of the Brassicaceae, 22:1 is virtually excluded from the sn-2 position of TAGs (Taylor 1994); thus erucic acid is essentially found only in the sn-3 and the sn-1 positions, limiting the potential overall proportions of 22:1 to a maximum of about 66 mol %. The best genetically-unmodified HEAR B. napus cultivars have only about 50% erucic acid in the seed oil.
In the traditional Kennedy pathway for seed oil (triacylglycerol, TAG) biosynthesis, lyso-phosphatidic acid acyltransferase (LPAT; EC 2.3.1.51) is the major enzyme responsible for acylating the sn-2 position of the glycerol backbone and therefore largely determines the sn-2 acyl composition of TAGs. This presumably ER-based LPAT is typically referred to as an LPAT2 in most oilseed species, distinguishing it from the plastidial LPAT1 which has enzyme characteristics more like the prokaryotic LPAT found in E. coli. 
Several studies have suggested that in B. napus this is at least partially due to the inability of the lyso-phosphatidic acid acyltransferase (LPAT; EC 2.3.1.51) to utilize erucoyl-CoA (Oo 1989; Bernerth 1990; Taylor 1990; Taylor 1992). Various groups worldwide have attempted or advocated the transformation of rapeseed with an LPAT gene which has the desired capacity to utilize erucoyl-CoA during TAG bioassembly (Cao 1990; Lohden 1990; Taylor 1990; Taylor 1992; Peterek 1992; Murphy 1994). LPATs from Limnanthes spp were originally cited as unique gene donors to accomplish this (Cao 1990; Lohden 1990; Taylor 1990; Taylor 1992; Peterek 1992; Murphy 1994). Accordingly, LPAT2s from L. douglasii and L. alba have been cloned and used to enhance sn-2 erucic proportions in B. napus (Brough 1996; Lassner 1995; Henke 1995) but with this single genetic modification, the enhancement of overall proportions of erucic acid and accumulation of significant trierucin have not resulted (Weier 1997). Indeed, the erucic acid was merely redistributed the sn-1 and sn-3 positions to the sn-2 position, with no significant improvement in the mol % erucic acid in seed TAGs.
There is a need to discover and characterize new higher plant LPATs which can utilize erucoyl-CoA or other VLC-CoAs and thereby be used to enhance erucic acid or other VLCFA (e.g. nervonic acid) content in organisms, especially plants, especially plants whose seed oils contain VLCFAs, more especially plants of the HEA Brassicaceae. There is a further need to discover plant LPATs which can enhance oil content of oilseeds in general.